Chemistry of the Hydrated Electron in Oxygen-Free Solutions of Amino Acids, Peptides, and Related Compounds

1967 ◽  
Vol 32 (3) ◽  
pp. 452 ◽  
Author(s):  
Rodney L. S. Willix ◽  
Warren M. Garrison
2001 ◽  
Vol 183 (18) ◽  
pp. 5441-5444 ◽  
Author(s):  
Hikaru Suenaga ◽  
Mariko Mitsuoka ◽  
Yuko Ura ◽  
Takahito Watanabe ◽  
Kensuke Furukawa

ABSTRACT Biphenyl dioxygenase (Bph Dox) catalyzes the initial oxygenation of biphenyl and related compounds. Bph Dox is a multicomponent enzyme in which a large subunit (encoded by the bphA1 gene) is significantly responsible for substrate specificity. By using the process of DNA shuffling of bphA1 of Pseudomonas pseudoalcaligenes KF707 and Burkholderia cepaciaLB400, a number of evolved Bph Dox enzymes were created. Among them, anEscherichia coli clone expressing chimeric Bph Dox exhibited extremely enhanced benzene-, toluene-, and alkylbenzene-degrading abilities. In this evolved BphA1, four amino acids (H255Q, V258I, G268A, and F277Y) were changed from the KF707 enzyme to those of the LB400 enzyme. Subsequent site-directed mutagenesis allowed us to determine the amino acids responsible for the degradation of monocyclic aromatic hydrocarbons.


2018 ◽  
Vol 165 (12) ◽  
Author(s):  
Tomoko Koito ◽  
Syuku Saitou ◽  
Toshihiro Nagasaki ◽  
Syosei Yamagami ◽  
Toshiro Yamanaka ◽  
...  

1965 ◽  
Vol 58 (4) ◽  
pp. 334-347 ◽  
Author(s):  
MIHOKO YOSHIDA ◽  
TADATOSHI KINOSHITA ◽  
SHIGEO HORIE ◽  
NORIO SHIMAZONO

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